Characterization of the two oligosaccharides present in the preferential hormonogenic domain of human thyroglobulin.
The N-terminal fragment of human thyroglobulin (residues 1 to 171) contains the preferential hormonogenic site of the molecule and 2 potential sites of N-glycosylation (Asn57 and Asn91). This fragment was isolated from a human thyroglobulin purified from a single goiter. The tryptic peptides bearing the glycosylation sites were separated by Bio-Gel P-30 and HPLC columns. The oligosaccharides borne at each site were analyzed, after tritium labeling, by concanavalin A-Sepharose and HPLC. At both sites the structures observed are heterogenous, with a majority of biantennary complex type structures.
Franc
J L
JL
URA 178 CNRS, Faculté de Médecine, Marseille, France.
Venot
N
N
Marriq
C
C
D002851:Chromatography, High Pressure Liquid; D005947:Glucose / Q000032:analysis; D006020:Glycopeptides / Q000302:isolation & purification; D006801:Humans; D008358:Mannose / Q000032:analysis; D009844:Oligosaccharides / Q000032:analysis*; D013954:Thyroglobulin / Q000032:analysis*; D013974:Thyroxine / Q000096:biosynthesis
D006020:Glycopeptides; D009844:Oligosaccharides; D013954:Thyroglobulin; D005947:Glucose; D008358:Mannose; D013974:Thyroxine